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4WFG

Human TRAAK K+ channel in a Tl+ bound conductive conformation

Functional Information from GO Data
ChainGOidnamespacecontents
A0005267molecular_functionpotassium channel activity
A0016020cellular_componentmembrane
A0071805biological_processpotassium ion transmembrane transport
B0005267molecular_functionpotassium channel activity
B0016020cellular_componentmembrane
B0071805biological_processpotassium ion transmembrane transport
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue TL A 301
ChainResidue
ATHR129
ATHR238
ATL307
BTHR129
BTHR238

site_idAC2
Number of Residues10
Detailsbinding site for residue TL A 302
ChainResidue
ATL303
ATL307
BILE130
BGLY131
BVAL239
BGLY240
AILE130
AGLY131
AVAL239
AGLY240

site_idAC3
Number of Residues9
Detailsbinding site for residue TL A 303
ChainResidue
AGLY131
ATYR132
AGLY240
APHE241
ATL302
BGLY131
BTYR132
BGLY240
BPHE241

site_idAC4
Number of Residues3
Detailsbinding site for residue TL A 304
ChainResidue
ACYS218
AASP222
ATRP223

site_idAC5
Number of Residues4
Detailsbinding site for residue CA A 305
ChainResidue
ASER112
AASP115
ASER118
AASP249

site_idAC6
Number of Residues6
Detailsbinding site for residue CA A 306
ChainResidue
AGLY98
AASP100
AHIS111
AHOH419
BGLU58
BHOH418

site_idAC7
Number of Residues10
Detailsbinding site for residue TL A 307
ChainResidue
ATHR129
AILE130
ATHR238
AVAL239
ATL301
ATL302
BTHR129
BILE130
BTHR238
BVAL239

site_idAC8
Number of Residues2
Detailsbinding site for residue TL B 303
ChainResidue
BCYS218
BTRP223

site_idAC9
Number of Residues3
Detailsbinding site for residue CA G 301
ChainResidue
GGLU10
GLYS19
GHOH407

Functional Information from PROSITE/UniProt
site_idPS00290
Number of Residues7
DetailsIG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YTCEATH
ChainResidueDetails
DTYR191-HIS197

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues46
DetailsTOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:22282805, ECO:0000269|PubMed:23341632, ECO:0000269|PubMed:25471887, ECO:0000269|PubMed:25500157
ChainResidueDetails
AMET27-SER29
AGLY177-ALA198
BMET27-SER29
BGLY177-ALA198

site_idSWS_FT_FI2
Number of Residues198
DetailsTRANSMEM: Helical => ECO:0000269|PubMed:22282805, ECO:0000269|PubMed:23341632, ECO:0000269|PubMed:25471887, ECO:0000269|PubMed:25500157
ChainResidueDetails
ATHR30-PHE50
ALEU144-ILE176
AMET199-MET220
ALEU260-VAL286
BTHR30-PHE50
BLEU144-ILE176
BMET199-MET220
BLEU260-VAL286

site_idSWS_FT_FI3
Number of Residues172
DetailsTOPO_DOM: Extracellular => ECO:0000269|PubMed:22282805, ECO:0000269|PubMed:23341632, ECO:0000269|PubMed:25471887, ECO:0000269|PubMed:25500157
ChainResidueDetails
AARG51-ALA113
AALA136-ARG143
AGLU221-LYS225
AALA246-PRO259
BARG51-ALA113
BALA136-ARG143
BGLU221-LYS225
BALA246-PRO259

site_idSWS_FT_FI4
Number of Residues28
DetailsINTRAMEM: Helical; Name=Pore helix 1 => ECO:0000269|PubMed:22282805, ECO:0000269|PubMed:23341632, ECO:0000269|PubMed:25471887, ECO:0000269|PubMed:25500157
ChainResidueDetails
ATRP114-THR128
BTRP114-THR128

site_idSWS_FT_FI5
Number of Residues22
DetailsINTRAMEM: INTRAMEM => ECO:0000269|PubMed:22282805, ECO:0000269|PubMed:23341632, ECO:0000269|PubMed:25471887, ECO:0000269|PubMed:25500157
ChainResidueDetails
ATHR129-VAL135
AGLY240-VAL245
BTHR129-VAL135
BGLY240-VAL245

site_idSWS_FT_FI6
Number of Residues26
DetailsINTRAMEM: Helical; Name=Pore helix 2 => ECO:0000269|PubMed:22282805, ECO:0000269|PubMed:23341632, ECO:0000269|PubMed:25471887, ECO:0000269|PubMed:25500157
ChainResidueDetails
ALEU226-VAL239
BLEU226-VAL239

site_idSWS_FT_FI7
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AGLN104
AGLN108
BGLN104
BGLN108

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PDB entries from 2024-07-24

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